1yqz

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[[Image:1yqz.gif|left|200px]]
[[Image:1yqz.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1yqz", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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{{STRUCTURE_1yqz| PDB=1yqz | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqz OCA], [http://www.ebi.ac.uk/pdbsum/1yqz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yqz RCSB]</span>
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'''Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution'''
'''Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution'''
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[[Category: Tsukihara, T.]]
[[Category: Tsukihara, T.]]
[[Category: Wallen, J R.]]
[[Category: Wallen, J R.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:40:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:18:37 2008''
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Revision as of 13:40, 3 May 2008

Template:STRUCTURE 1yqz

Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution


Overview

Coenzyme A (CoASH) replaces glutathione as the major low molecular weight thiol in Staphylococcus aureus; it is maintained in the reduced state by coenzyme A-disulfide reductase (CoADR), a homodimeric enzyme similar to NADH peroxidase but containing a novel Cys43-SSCoA redox center. The crystal structure of S. aureus CoADR has been solved using multiwavelength anomalous dispersion data and refined at a resolution of 1.54 A. The resulting electron density maps define the Cys43-SSCoA disulfide conformation, with Cys43-S(gamma) located at the flavin si face, 3.2 A from FAD-C4aF, and the CoAS- moiety lying in an extended conformation within a cleft at the dimer interface. A well-ordered chloride ion is positioned adjacent to the Cys43-SSCoA disulfide and receives a hydrogen bond from Tyr361'-OH of the complementary subunit, suggesting a role for Tyr361' as an acid-base catalyst during the reduction of CoAS-disulfide. Tyr419'-OH is located 3.2 A from Tyr361'-OH as well and, based on its conservation in known functional CoADRs, also appears to be important for activity. Identification of residues involved in recognition of the CoAS-disulfide substrate and in formation and stabilization of the Cys43-SSCoA redox center has allowed development of a CoAS-binding motif. Bioinformatics analyses indicate that CoADR enzymes are broadly distributed in both bacterial and archaeal kingdoms, suggesting an even broader significance for the CoASH/CoAS-disulfide redox system in prokaryotic thiol/disulfide homeostasis.

About this Structure

1YQZ is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution., Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A, Biochemistry. 2006 Sep 26;45(38):11278-89. PMID:16981688 Page seeded by OCA on Sat May 3 16:40:21 2008

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